Evidence map›Paper›PMID 18583528›Full record

ArticlePlant physiology2008

Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis.

Panagiotis N Moschou, Maite Sanmartin, Athina H Andriopoulou, Enrique Rojo, Jose J Sanchez-Serrano, Kalliopi A Roubelakis-Angelakis

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
5.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

75 citing papers in PubMed, 199 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Genome-Wide Identification of Polyamine Oxidase (PAO) Family Genes: Roles ofInternational journal of molecular sciences · 2022
    Article
  8. Polyamine Oxidase Triggers HInternational journal of molecular sciences · 2022
    Article
  9. Article
  10. Effect of thermospermine on expression profiling of different gene using massive analysis of cDNA ends (MACE) and vascular maintenance in Arabidopsis.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Article
  11. Frontiers in plant science · 2021
    Article
  12. Article
  13. The tree of life of polyamine oxidases.Scientific reports · 2020
    Article
  14. uORFs: ImportantInternational journal of molecular sciences · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Plant Peroxisomes: A Factory of Reactive Species.Frontiers in plant science · 2020
    Review
  19. Article
  20. Review

15 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Panagiotis N MoschouDepartment of Biology, University of Crete, 71409 Heraklion, Greece.
Maite Sanmartin
Athina H Andriopoulou
Enrique Rojo
Jose J Sanchez-Serrano
Kalliopi A Roubelakis-Angelakis
Consejo Superior de Investigaciones Científicas · ESCentro Nacional de Biotecnología · ESUniversity of Crete · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In contrast to animals, where polyamine (PA) catabolism efficiently converts spermine (Spm) to putrescine (Put), plants have been considered to possess a PA catabolic pathway producing 1,3-diaminopropane, Delta(1)-pyrroline, the corresponding aldehyde, and hydrogen peroxide but unable to back-convert Spm to Put. Arabidopsis (Arabidopsis thaliana) genome contains at least five putative PA oxidase (PAO) members with yet-unknown localization and physiological role(s). AtPAO1 was recently identified as an enzyme similar to the mammalian Spm oxidase, which converts Spm to spermidine (Spd). In this work, we have performed in silico analysis of the five Arabidopsis genes and have identified PAO3 (AtPAO3) as a nontypical PAO, in terms of homology, compared to other known PAOs. We have expressed the gene AtPAO3 and have purified a protein corresponding to it using the inducible heterologous expression system of Escherichia coli. AtPAO3 catalyzed the sequential conversion/oxidation of Spm to Spd, and of Spd to Put, thus exhibiting functional homology to the mammalian PAOs. The best substrate for this pathway was Spd, whereas the N(1)-acetyl-derivatives of Spm and Spd were oxidized less efficiently. On the other hand, no activity was detected when diamines (agmatine, cadaverine, and Put) were used as substrates. Moreover, although AtPAO3 does not exhibit significant similarity to the other known PAOs, it is efficiently inhibited by guazatine, a potent PAO inhibitor. AtPAO3 contains a peroxisomal targeting motif at the C terminus, and it targets green fluorescence protein to peroxisomes when fused at the N terminus but not at the C terminus. These results reveal that AtPAO3 is a peroxisomal protein and that the C terminus of the protein contains the sorting information. The overall data reinforce the view that plants and mammals possess a similar PA oxidation system, concerning both the subcellular localization and the mode of its action.

Indexed as

Abscisic AcidAmino Acid SequenceAnimalsArabidopsisArabidopsis ProteinsCloning, MolecularCyclopentanesFlavin-Adenine DinucleotideGreen Fluorescent ProteinsKineticsMammalsMolecular Sequence DataOxidoreductases Acting on CH-NH Group DonorsOxylipinsPeroxisomesPhylogenyAbscisic AcidArabidopsis ProteinsCyclopentanesFlavin-Adenine DinucleotideGreen Fluorescent Proteinsjasmonic acidOxidoreductases Acting on CH-NH Group DonorsOxylipinsPlant Growth RegulatorsPolyamine OxidasePolyaminesRecombinant Fusion Proteins

Identifiers

PMID18583528
PMCPMC2492618
OpenAlexW2077361793

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.